ID K0RN37_THAOC Unreviewed; 1038 AA.
AC K0RN37;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
DE Flags: Fragment;
GN ORFNames=THAOC_33072 {ECO:0000313|EMBL:EJK48157.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK48157.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK48157.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK48157.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|ARBA:ARBA00001928};
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJK48157.1}.
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DR EMBL; AGNL01046208; EJK48157.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RN37; -.
DR EnsemblProtists; EJK48157; EJK48157; THAOC_33072.
DR eggNOG; KOG1562; Eukaryota.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR GO; GO:0010487; F:thermospermine synthase activity; IEA:UniProt.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 144..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..702
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 111..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
FT NON_TER 1038
FT /evidence="ECO:0000313|EMBL:EJK48157.1"
SQ SEQUENCE 1038 AA; 116086 MW; A51E8CDF3E494D07 CRC64;
MDRSARSSPS TIDRAWYVPL QSNTYLHQPS CQQPSCERSC GPSAGKHDTY RQYAAAWDRA
YTDADRYVVS TWYICRLEER CQDRSKRQIP NPHRAEEDKN YSSDNMVIQR ADRPAARGKR
DIPNRGAGED MSSKGGRKLR VFEINLSVGF ILLSIALSAT VAFSVGVVLN VYAIGARTPG
PESDRDFFEA PDAPLDVRGT SLPTSSIVTT KVVYKTKSSG DEPDASSERN YFSCAIHSAE
EDGDDDSEDD ESSSDDSEDG EEREEKLSNS SGQQLFLEME GASPDFLASK ESLMKAMYKI
ASAAQPSVDT SVTTQCYSYE GGKVYCGGFI QDSQFAIHTA PGSGKMSFDI FTCGKSDLID
LVPTVKELLV LNHLSGDDVK PRIRWSHWLR GFRHEDDAQI DPHLVPLEQD LGDDVSGLSD
VKEIVVSRTT SFQRVDIISM LNRESHQIGA EEKYYQRYLK SLSRDGSYES LHPEFFQPDR
ILYLDGVLQS TLYGDAPYHE SLVHPAMIAH PNPKRVAIIG GGEGATLREV LKHKTVEKVV
MVEIDGELVE LCTEYLPQWN RCDDIQGSTE ICFDDPRAQV DFRDAFAWFI DSFGDKDNLK
DEQFDVIIMD ALDPDRFVDI VGSLYKNDLF VQSLFNGLKD DGVFVVQLGE TDYVDDPPYQ
SMAPDTALML DTIKSAGFDS MVNYENPHCF FGAPWTFMVS FKNYNTRSRW YRSSAEIEID
LHSRILSTKS GKPPLRYIDG SSMAEQQTPR PALERVYCRK SKLPWECQYD WFGVDLSSRA
IHIAPATWNL MQSNKSGSGM AELLDLAKST NFIPLGDQYM ILGTGEDTPL SDNMADGKVP
VYTQLFATGV FSPNTEMMRK GLGEIRRRTD MDRSWMVVRE VQPENELFSS VNGAIAEPTR
GARTLPYDRA TDQPTDQVIK TRRVHLPDLA IFGLRQRRRR SVTRDSGKTA RDWVLSTSDG
ADKSTTDDAM MVVFEVDGCH GLTRTDPLDP SVCCREDTQP SRIDPSAPRT LLAAGKKFIG
IIGSGPGLEI SKTYDLSI
//
